Purification, crystallization and preliminary X-ray analysis of the inverse F-BAR domain of the human srGAP2 protein.
Purification, crystallization and preliminary X-ray analysis of the inverse F-BAR domain of the human srGAP2 protein.
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DOI：
10.1107/s2053230x13033712
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发表时间：
2014
期刊：
影响因子：
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通讯作者：
Hongpeng Wang;Yan Zhang;Zhenyi Zhang;W. Jin;Geng Wu
中科院分区：
文献类型：
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作者：
Hongpeng Wang;Yan Zhang;Zhenyi Zhang;W. Jin;Geng Wu
BAR结构域蛋白通过诱导膜内陷或膜突起，在多种细胞过程中发挥重要作用。在BAR超家族中，‘经典’BAR和Fes/CIP4同源BAR(F-bar)亚家族蛋白通常促进膜内陷，而反向BAR(I-bar)亚家族通常促进膜突起。尽管SRGAP2蛋白具有N-末端的F-bar结构域，但它通过引起膜突起来调节轴突生长和神经元迁移，这使人想起I-bar结构域蛋白的活性。在本研究中，我们对人SRGAP2的反F-bar(IF-bar)结构域进行了高效表达、纯化和结晶。SRGAP2 IF-bar结构域蛋白的晶体衍射率达到3.50ä，属于空间群P2(1)。这些结果将有助于进一步确定SRGAP2的IF-bar结构域的结构，并最终阐明其诱导膜突起而不是膜内陷的特殊行为。
Bin-Amphiphysin-Rvs (BAR) domain proteins play essential roles in diverse cellular processes by inducing membrane invaginations or membrane protrusions. Among the BAR superfamily, the `classical' BAR and Fes/CIP4 homology BAR (F-BAR) subfamilies of proteins usually promote membrane invaginations, whereas the inverse BAR (I-BAR) subfamily generally incur membrane protrusions. Despite possessing an N-terminal F-BAR domain, the srGAP2 protein regulates neurite outgrowth and neuronal migration by causing membrane protrusions reminiscent of the activity of I-BAR domain proteins. In this study, the inverse F-BAR (IF-BAR) domain of human srGAP2 was overexpressed, purified and crystallized. The crystals of the srGAP2 IF-BAR domain protein diffracted to 3.50 Å resolution and belonged to space group P2(1). These results will facilitate further structural determination of the srGAP2 IF-BAR domain and the ultimate elucidation of its peculiar behaviour of inducing membrane protrusions rather than membrane invaginations.